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dc.contributor.authorJemil, Ineses_ES
dc.contributor.authorMora, Leticiaes_ES
dc.contributor.authorNasri, Rimes_ES
dc.contributor.authorAbdelhedi, Olaes_ES
dc.contributor.authorAristoy, María Concepciónes_ES
dc.contributor.authorHajji, Mohamedes_ES
dc.contributor.authorNasri, Moncefes_ES
dc.contributor.authorToldrá Vilardell, Fideles_ES
dc.date.accessioned2017-11-02T13:26:26Z-
dc.date.available2017-11-02T13:26:26Z-
dc.date.issued2016-08-24-
dc.identifier.citationFood Research International 89 (1): 347-358 (2016)es_ES
dc.identifier.issn0963-9969-
dc.identifier.urihttp://hdl.handle.net/10261/156964-
dc.description.abstractAntioxidant and angiotensin I-converting enzyme (ACE)-inhibitory activities of sardinelle (Sardinella aurita) protein hydrolysates (SPHs) obtained by fermentation with Bacillus subtilis A26 (SPH-A26) and Bacillus amyloliquefaciens An6 (SPH-An6) were investigated. Both hydrolysates showed dose-dependent antioxidant activities evaluated using various in vitro antioxidant assays. Further, they were found to exhibit ACE-inhibitory activity. Peptides from SPH-A26 and SPH-An6 were analyzed by nESI-LC–MS/MS and approximately 800 peptides were identified. Identified peptides derived mainly from myosin (43% and 31% in SPH-An6 and SPH-A26, respectively). Several peptides identified in both hydrolysates were found to share sequences with previously identified antioxidant and ACE-inhibitory peptides based on Biopep database. Some of these peptides were selected for synthesis and their biological activities were evaluated. Among the synthesized peptides, NVPVYEGY and ITALAPSTM were found to be the most effective ACE-inhibitors with IC50 values of 0.21 and 0.23 mM, respectively. On the other hand, NVPVYEGY, which exhibited the highest ACE-inhibitory activity, showed the highest reducing power and peroxyl radical scavenging activities, followed by SLEAQAEKY and GTEDELDKY. The results of this study suggest that fermented sardinelle protein hydrolysates are a good source of natural antioxidant peptides and could have the potential to act as hypotensive nutraceutical ingredients.es_ES
dc.description.sponsorshipThis work was funded by grant AGL2014-57367-R from MINECO and FEDER funds as well as the Ministry of Higher Education and Scientific Research-Tunisia and the Emerging Research Group Grant from Generalitat Valenciana in Spain (GV/2015/138). JAEDOC-CSIC postdoctoral contract of L.M. cofunded by the European Social Found is also acknowledged. LC-MS/MS analysis was carried out in the SCSIE University of Valencia Proteomics Unit (Spain), a member of ISCIII ProteoRed Proteomics Platform.es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2014-57367-Res_ES
dc.relation.isversionofPostprintes_ES
dc.rightsopenAccesses_ES
dc.subjectSardinella auritaes_ES
dc.subjectFermentationes_ES
dc.subjectProtein hydrolysateses_ES
dc.subjectAntioxidant activityes_ES
dc.subjectACE-inhibitory activityes_ES
dc.subjectPeptidomic analysises_ES
dc.titleA peptidomic approach for the identification of antioxidant and ACE-inhibitory peptides in sardinelle protein hydrolysates fermented by Bacillus subtilis A26 and Bacillus amyloliquefaciens An6es_ES
dc.typeartículoes_ES
dc.identifier.doi10.1016/j.foodres.2016.08.020-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://doi.org/10.1016/j.foodres.2016.08.020es_ES
dc.rights.licensehttp://creativecommons.org/licenses/by-nc-nd/4.0/es_ES
dc.contributor.funderGeneralitat Valencianaes_ES
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.contributor.funderMinistère de l’Enseignement Supérieur et de la Recherche Scientifique (Tunisie)es_ES
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)es_ES
dc.contributor.funderEuropean Commissiones_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003359es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.cerifentitytypePublications-
item.languageiso639-1en-
item.grantfulltextopen-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextWith Fulltext-
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